KCNT2_RAT
ID KCNT2_RAT Reviewed; 1142 AA.
AC Q6UVM4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Potassium channel subfamily T member 2;
DE AltName: Full=Sequence like an intermediate conductance potassium channel subunit;
DE AltName: Full=Sodium and chloride-activated ATP-sensitive potassium channel Slo2.1;
GN Name=Kcnt2; Synonyms=Slick;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLY-1032, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=14684870; DOI=10.1523/jneurosci.23-37-11681.2003;
RA Bhattacharjee A., Joiner W.J., Wu M., Yang Y., Sigworth F.J.,
RA Kaczmarek L.K.;
RT "Slick (Slo2.1), a rapidly-gating sodium-activated potassium channel
RT inhibited by ATP.";
RL J. Neurosci. 23:11681-11691(2003).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15717307; DOI=10.1002/cne.20462;
RA Bhattacharjee A., von Hehn C.A.A., Mei X., Kaczmarek L.K.;
RT "Localization of the Na+-activated K+ channel Slick in the rat central
RT nervous system.";
RL J. Comp. Neurol. 484:80-92(2005).
RN [3]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16687497; DOI=10.1523/jneurosci.3372-05.2006;
RA Santi C.M., Ferreira G., Yang B., Gazula V.R., Butler A., Wei A.,
RA Kaczmarek L.K., Salkoff L.;
RT "Opposite regulation of Slick and Slack K+ channels by neuromodulators.";
RL J. Neurosci. 26:5059-5068(2006).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17699666; DOI=10.1523/jneurosci.0551-07.2007;
RA Berg A.P., Sen N., Bayliss D.A.;
RT "TrpC3/C7 and Slo2.1 are molecular targets for metabotropic glutamate
RT receptor signaling in rat striatal cholinergic interneurons.";
RL J. Neurosci. 27:8845-8856(2007).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF PHE-240.
RX PubMed=29069600; DOI=10.1016/j.celrep.2017.09.088;
RA Gururaj S., Palmer E.E., Sheehan G.D., Kandula T., Macintosh R., Ying K.,
RA Morris P., Tao J., Dias K.R., Zhu Y., Dinger M.E., Cowley M.J., Kirk E.P.,
RA Roscioli T., Sachdev R., Duffey M.E., Bye A., Bhattacharjee A.;
RT "A De Novo Mutation in the Sodium-Activated Potassium Channel KCNT2 Alters
RT Ion Selectivity and Causes Epileptic Encephalopathy.";
RL Cell Rep. 21:926-933(2017).
CC -!- FUNCTION: Outward rectifying potassium channel. Produces rapidly
CC activating outward rectifier K(+) currents. Activated by high
CC intracellular sodium and chloride levels (PubMed:14684870,
CC PubMed:29069600). Channel activity is inhibited by ATP and by
CC inhalation anesthetics, such as isoflurane (PubMed:17699666). Inhibited
CC upon stimulation of G-protein coupled receptors, such as CHRM1 and GRM1
CC (By similarity). {ECO:0000250|UniProtKB:Q6UVM3,
CC ECO:0000269|PubMed:14684870, ECO:0000269|PubMed:17699666,
CC ECO:0000269|PubMed:29069600}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15717307,
CC ECO:0000269|PubMed:16687497}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in brain, and at low levels in heart.
CC Detected in brainstem, including auditory neurons such as the medial
CC nucleus of the trapezoid body. Detected in the olfactory bulb, red
CC nucleus, facial nucleus, pontine nucleus, oculomotor nucleus,
CC substantia nigra, deep cerebellar nuclei, vestibular nucleus, and the
CC thalamus. Detected in hippocampal CA1, CA2, and CA3 regions, the
CC dentate gyrus, supraoptic nucleus, hypothalamus, dorsal root ganglion,
CC and cortical layers II, III, and V. Detected in striatum cholinergic
CC interneurons. {ECO:0000269|PubMed:14684870,
CC ECO:0000269|PubMed:15717307, ECO:0000269|PubMed:16687497,
CC ECO:0000269|PubMed:17699666}.
CC -!- PTM: Phosphorylated by protein kinase C. Phosphorylation inhibits
CC channel activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the potassium channel family. Calcium-activated
CC (TC 1.A.1.3) subfamily. KCa4.2/KCNT2 sub-subfamily. {ECO:0000305}.
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DR EMBL; AY359443; AAR06169.1; -; mRNA.
DR RefSeq; NP_942057.1; NM_198762.1.
DR AlphaFoldDB; Q6UVM4; -.
DR SMR; Q6UVM4; -.
DR STRING; 10116.ENSRNOP00000017884; -.
DR GlyGen; Q6UVM4; 1 site.
DR PaxDb; Q6UVM4; -.
DR PRIDE; Q6UVM4; -.
DR ABCD; Q6UVM4; 1 sequenced antibody.
DR GeneID; 304827; -.
DR KEGG; rno:304827; -.
DR UCSC; RGD:735074; rat.
DR CTD; 343450; -.
DR RGD; 735074; Kcnt2.
DR VEuPathDB; HostDB:ENSRNOG00000013312; -.
DR eggNOG; KOG3193; Eukaryota.
DR InParanoid; Q6UVM4; -.
DR OMA; QATYYVV; -.
DR OrthoDB; 858812at2759; -.
DR PhylomeDB; Q6UVM4; -.
DR PRO; PR:Q6UVM4; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000013312; Expressed in frontal cortex and 10 other tissues.
DR ExpressionAtlas; Q6UVM4; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; TAS:RGD.
DR GO; GO:0070089; F:chloride-activated potassium channel activity; IMP:UniProtKB.
DR GO; GO:0005228; F:intracellular sodium activated potassium channel activity; IBA:GO_Central.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; IDA:MGI.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IMP:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; IDA:MGI.
DR InterPro; IPR003929; K_chnl_BK_asu.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF03493; BK_channel_a; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Nucleotide-binding; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1142
FT /note="Potassium channel subfamily T member 2"
FT /id="PRO_0000312504"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..173
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 229..249
FT /note="Pore-forming"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..1142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 422..550
FT /note="RCK N-terminal"
FT REGION 989..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1020
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1032..1039
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 240
FT /note="F->L: Loss of chloride-activated potassium channel
FT activity. Loss of potassium selectivity. Inhibited by
FT chloride. Expression in primary dorsal root ganglion
FT neurons induces membrane hyperexcitability and neuronal
FT toxicity."
FT /evidence="ECO:0000269|PubMed:29069600"
FT MUTAGEN 1032
FT /note="G->S: Loss of channel inactivation by ATP."
FT /evidence="ECO:0000269|PubMed:14684870"
SQ SEQUENCE 1142 AA; 131100 MW; C4CF38B135A61C18 CRC64;
MVDLESEVPP LPPRYRFRDL LLGDQGWQND DRVQVEFYMN ENTFKERLKL FFIKNQRSSL
RIRLFNFSLK LLSCLLYIIR VLLEKPSQGN DWSHIFWVNR SLPLWGLQVS VALISLFETI
LLGYLSYKGN IWEQILRVPF ILEIINAVPF IISIFWPTLR NLFVPVFLNC WLAKHALENM
INDLHRAIQR TQSAMFNQVL ILISTLLCLI FTCICGIQHL ERIGKKLNLF DSLYFCIVTF
STVGFGDVTP ETWSSKLFVV AMICVALVVL PIQFEQLAYL WMERQKSGGN YSRHRAQTEK
HVVLCVSSLK IDLLMDFLNE FYAHPRLQDY YVVILCPTEM DVQVRRVLQI PMWSQRVIYL
QGSALKDQDL LRAKMDNAEA CFILSSRCEV DRTSSDHQTI LRAWAVKDFA PNCPLYVQIL
KPENKFHIKF ADHVVCEEEF KYAMLALNCI CPATSTLITL LVHTSRGQCV CLCCREGQQS
PEQWQKTYGR CSGNEVYHIV LEESTFFAEY EGKSFTYASF HAHKKFGVCL VGVRREDNKN
ILLNPGPRYI MNASDICFYI NITKEENSAF KNQDQQRKSN VSRSFYHGPS RLPVHSIIAS
MGTVAIDLQD TSCRAASGPT LALPSEGGKE LRRPSIAPVL EVADTSSIQT CDLLSDQSED
ETTPDEETSS NLEYAKGYPP YSPYIGSSPT FCHLLQEKVP FCCLRLDKSC QHNYYEDAKA
YGFKNKLIIV AAETAGNGLY NFIVPLRAYY RPKKELNPIV LLLDNPPDMH FLDAICWFPM
VYYMVGSIDN LDDLLRCGVT FAANMVVVDK ESTMSAEEDY MADAKTIVNV QTLFRLFSSL
SIITELTHPA NMRFMQFRAK DCYSLALSKL EKKERERGSN LAFMFRLPFA AGRVFSISML
DTLLYQSFVK DYMISITRLL LGLDTIPGSG FLCSMKITED DLWIRTYARL YQKLCSSTGD
VPIGIYRTES QKLTTSESQI SISVEEWEDT KDVKDPGHHR SIHRNSTSSD QSDHPLLRRK
SMQWARRLSR KGPKHSGKTA EKITQQRLNL YRRSERQELA ELVKNRMKHL GLSTVGYDEM
NDHQSTLSYI LINPSPDTRL ELNDVVYLIR PDPLSYLPNS EPSRKNSICN AAVQDSREET
QL
